Cloned (Comment) | Organism |
---|---|
orf PH0655, amino acid sequence determination and analysis, expression of His-tagged enzyme in Escherichia coli strain TOP10 | Pyrococcus horikoshii |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
L-2-amino-3-oxobutyrate | competitive product inhibition by the unstable L-2-amino-3-oxobutyrate only in presence of NADH, which stabilizes | Pyrococcus horikoshii |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Co2+ | can replace Zn2+ with 35% of the activity with Zn2+ | Pyrococcus horikoshii | |
Mn2+ | can replace Zn2+ with 77% of the activity with Zn2+ | Pyrococcus horikoshii | |
Zn2+ | required | Pyrococcus horikoshii |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
41200 | - |
4 * 41200, recombinant enzyme, SDS-PAGE, 4 * 41815, sequence calculation | Pyrococcus horikoshii |
41815 | - |
4 * 41200, recombinant enzyme, SDS-PAGE, 4 * 41815, sequence calculation | Pyrococcus horikoshii |
192000 | - |
recombinant enzyme, gel filtration | Pyrococcus horikoshii |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-threonine + NAD+ | Pyrococcus horikoshii | - |
(2S)-2-amino-3-oxobutanoate + NADH + H+ | - |
? | |
L-threonine + NAD+ | Pyrococcus horikoshii OT-3 | - |
(2S)-2-amino-3-oxobutanoate + NADH + H+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pyrococcus horikoshii | - |
strain OT3 | - |
Pyrococcus horikoshii OT-3 | - |
strain OT3 | - |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme from Escherichia coli strain TOP10 by nickel affinity chromatography | Pyrococcus horikoshii |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
L-threonine + NAD+ = L-2-amino-3-oxobutanoate + NADH + H+ | reaction mechanism, random bi bi kinetic mechanism | Pyrococcus horikoshii |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
3.43 | - |
purified recombinant enzyme | Pyrococcus horikoshii |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
DL-threo-3-phenylserine + NAD+ | 53% of the activity with L-threonine | Pyrococcus horikoshii | ? + NADH | - |
? | |
DL-threo-3-phenylserine + NAD+ | 53% of the activity with L-threonine | Pyrococcus horikoshii OT-3 | ? + NADH | - |
? | |
L-serine + NAD+ | 21% of the activity with L-threonine | Pyrococcus horikoshii | ? + NADH | - |
? | |
L-serine + NAD+ | 21% of the activity with L-threonine | Pyrococcus horikoshii OT-3 | ? + NADH | - |
? | |
L-threonine + NAD+ | - |
Pyrococcus horikoshii | (2S)-2-amino-3-oxobutanoate + NADH + H+ | - |
? | |
L-threonine + NAD+ | stereospecificity, overview | Pyrococcus horikoshii | (2S)-2-amino-3-oxobutanoate + NADH + H+ | - |
? | |
L-threonine + NAD+ | - |
Pyrococcus horikoshii OT-3 | (2S)-2-amino-3-oxobutanoate + NADH + H+ | - |
? | |
L-threonine + NAD+ | stereospecificity, overview | Pyrococcus horikoshii OT-3 | (2S)-2-amino-3-oxobutanoate + NADH + H+ | - |
? | |
additional information | substrate specificity, overview | Pyrococcus horikoshii | ? | - |
? | |
additional information | substrate specificity, overview | Pyrococcus horikoshii OT-3 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
tetramer | 4 * 41200, recombinant enzyme, SDS-PAGE, 4 * 41815, sequence calculation | Pyrococcus horikoshii |
Synonyms | Comment | Organism |
---|---|---|
L-ThrDH | - |
Pyrococcus horikoshii |
L-threonine dehydrogenase | - |
Pyrococcus horikoshii |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
70 | - |
- |
Pyrococcus horikoshii |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
80 | - |
60 min, pH 7.0, over 90% remaining activity, purified recombinant enzyme | Pyrococcus horikoshii |
100 | - |
30 min, pH 7.0, over 90% remaining activity, purified recombinant enzyme | Pyrococcus horikoshii |
105 | - |
higher loss of activity above, purified recombinant enzyme | Pyrococcus horikoshii |
120 | - |
20 min, inactivation, purified recombinant enzyme | Pyrococcus horikoshii |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
10 | - |
- |
Pyrococcus horikoshii |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
9.2 | 12 | 22% of maximal activity at pH 9.2, 50% at pH 9.5, and 52% at pH 12.0 | Pyrococcus horikoshii |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Pyrococcus horikoshii |